Identification of Mycoplasma pneumoniae proteins associated with hemadsorption and virulence.
Twenty-two mutants of Mycoplasma pneumoniae spontaneously deficient in hemadsorption were isolated. Examination of mutant protein profiles by one- and two-dimensional polyacrylamide gel electrophoresis permitted the grouping of these mutants into four classes. The largest class of mutants was deficient in four high-molecular-weight proteins (215,000, 210,000, 190,000, and 140,000). A second class of mutants lacked three proteins previously designated A, B, and C (72,000, 85,000, and 37,000, respectively). A single mutant, in addition to lacking proteins A, B, and C, was missing a fourth protein of 165,000 molecular weight. The remaining mutants exhibited protein profiles apparently identical to that of the wild-type strain. All mutant strains attached to the respiratory epithelium of hamster tracheal rings in vitro at reduced levels; however, mutants lacking proteins A, B, and C recognized only neuraminidase-insensitive receptors. None of the mutants tested produced detectable pneumonia in intranasally inoculated hamsters, although one mutant class demonstrated low-level survival in vivo.
D000268:Adhesiveness; D000818:Animals; D001426:Bacterial Proteins / Q000502:physiology*; D006224:Cricetinae; D006382:Hemadsorption; D008970:Molecular Weight; D009154:Mutation; D009177:Mycoplasma pneumoniae / Q000032:analysis / Q000235:genetics / Q000472:pathogenicity*; D009439:Neuraminidase / Q000494:pharmacology; D014132:Trachea / Q000382:microbiology*
D001426:Bacterial Proteins; D009439:Neuraminidase